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Full-Text Articles in Physical Sciences and Mathematics
Metalation And Structural Properties Of Apo-Metallothioneins, Gordon W. Irvine
Metalation And Structural Properties Of Apo-Metallothioneins, Gordon W. Irvine
Electronic Thesis and Dissertation Repository
Metals are required by a quarter of all proteins to achieve their biological function, whether in an active site involved in catalytic chemistry or in a structural capacity. Metals are tightly regulated at the cellular level due to their propensity to cause unwanted side reactions and to be scavenged for use by pathogens. One of the proteins involved in this regulation of metal homeostasis is metallothionein (MT) which is a small, cysteine rich protein primarily involved in the regulation of zinc and copper homeostasis and heavy metal detoxification. MT is unique in its high cysteine content (~30% of the residues), …
Reactions Between Zinc Metallothionein And Carbonic Anhydrase, Tyler B. J. Pinter
Reactions Between Zinc Metallothionein And Carbonic Anhydrase, Tyler B. J. Pinter
Electronic Thesis and Dissertation Repository
More than 25% of proteins require metal ion cofactors for structure or function. The interactions between metalloproteins have largely been overlooked, though these interactions ultimately govern metal localization and control metal ion homeostasis. Mammalian metallothionein (MT) is a small, cysteine-rich metalloprotein that binds numerous metal ions per protein strand. Up to seven divalent metals, such as zinc or cadmium, are wrapped into a clustered two-domain structure. This unusually high metal content places MT as an attractive candidate for studying interactions with other metal-binding proteins. This present study investigates the metal transfer reactions between MTs and other metalloproteins, using carbonic anhydrase …
The Role Of Metallothionein In Zinc Homeostasis, Kelly L. Summers
The Role Of Metallothionein In Zinc Homeostasis, Kelly L. Summers
Electronic Thesis and Dissertation Repository
The structure of the unique metal-binding protein, metallothionein (MT), consists of two metal-thiolate-clustered binding domains; the β-domain binds up to three divalent metals and the α-domain binds four. The mechanisms through which the metals are bound and arranged into domains, as well as the function of MT in metal ion homeostasis, remains largely unknown. By utilizing electrospray ionization mass spectrometry (ESI MS) to identify each species, and by comparing the data with simulations, MT 1a was found to bind Zn2+ non-cooperatively. Through a competition experiment between MT and its individual domain peptides, MT was proposed to bind Zn2+ …